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Database: UniProt
Entry: G8BTQ9_TETPH
LinkDB: G8BTQ9_TETPH
Original site: G8BTQ9_TETPH 
ID   G8BTQ9_TETPH            Unreviewed;       331 AA.
AC   G8BTQ9;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   24-JAN-2024, entry version 45.
DE   RecName: Full=Manganese/iron superoxide dismutase C-terminal domain-containing protein {ECO:0000259|Pfam:PF02777};
GN   Name=TPHA0E01950 {ECO:0000313|EMBL:CCE63287.1};
GN   OrderedLocusNames=TPHA_0E01950 {ECO:0000313|EMBL:CCE63287.1};
OS   Tetrapisispora phaffii (strain ATCC 24235 / CBS 4417 / NBRC 1672 / NRRL
OS   Y-8282 / UCD 70-5) (Yeast) (Fabospora phaffii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Tetrapisispora.
OX   NCBI_TaxID=1071381 {ECO:0000313|EMBL:CCE63287.1, ECO:0000313|Proteomes:UP000005666};
RN   [1] {ECO:0000313|EMBL:CCE63287.1, ECO:0000313|Proteomes:UP000005666}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24235 / CBS 4417 / NBRC 1672 / NRRL Y-8282 / UCD 70-5
RC   {ECO:0000313|Proteomes:UP000005666};
RX   PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA   Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA   Wolfe K.H.;
RT   "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT   accidents.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
CC   -!- FUNCTION: Component of the mitochondrial ribosome (mitoribosome), a
CC       dedicated translation machinery responsible for the synthesis of
CC       mitochondrial genome-encoded proteins, including at least some of the
CC       essential transmembrane subunits of the mitochondrial respiratory
CC       chain. The mitoribosomes are attached to the mitochondrial inner
CC       membrane and translation products are cotranslationally integrated into
CC       the membrane. {ECO:0000256|ARBA:ARBA00037226}.
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DR   EMBL; HE612860; CCE63287.1; -; Genomic_DNA.
DR   RefSeq; XP_003685721.1; XM_003685673.1.
DR   AlphaFoldDB; G8BTQ9; -.
DR   STRING; 1071381.G8BTQ9; -.
DR   GeneID; 11531268; -.
DR   KEGG; tpf:TPHA_0E01950; -.
DR   eggNOG; KOG0876; Eukaryota.
DR   HOGENOM; CLU_057349_0_0_1; -.
DR   OMA; LENCWEC; -.
DR   OrthoDB; 2055478at2759; -.
DR   Proteomes; UP000005666; Chromosome 5.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0004784; F:superoxide dismutase activity; IEA:InterPro.
DR   Gene3D; 3.55.40.20; Iron/manganese superoxide dismutase, C-terminal domain; 1.
DR   InterPro; IPR019832; Mn/Fe_SOD_C.
DR   InterPro; IPR036314; SOD_C_sf.
DR   PANTHER; PTHR43595:SF1; 37S RIBOSOMAL PROTEIN MRP1, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43595; 37S RIBOSOMAL PROTEIN S26, MITOCHONDRIAL; 1.
DR   Pfam; PF02777; Sod_Fe_C; 1.
DR   SUPFAM; SSF54719; Fe,Mn superoxide dismutase (SOD), C-terminal domain; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005666}.
FT   DOMAIN          268..319
FT                   /note="Manganese/iron superoxide dismutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02777"
FT   COILED          235..269
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   331 AA;  38344 MW;  6E308683A20AFC4E CRC64;
     MSYILVTKKI VSSLIRAHVI TRSYITPSLD HLNEKDGLPG LYSSQGLRNA WYERVQHHTD
     ELNKFVDENT DERPILQLIN DHSKSFTKRN LVKNAAMIHN LTFANNSLTA SNVNFDYQLP
     LANKKTTLIK DSVDIKLNYK NEPDKITYKK LYPAILSSFG SMVEFRTLLL NSNLGISGDG
     FTWLVARKHQ AYDYSMESSN YSEVKFDRLF VVNTYNAGTP FNFNKSNQMT ELKLFQEKEL
     KTQQTEEQIE ELAKKDENKE KDINDVLEAH SYDKNVSYIP LLAIDASPKC WLHDYGVFGK
     EQYLNNVWES INWDVVESRM PELSQQYKVV I
//
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